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Molecular cloning and expression of an extracellular α-amylase gene from an Antarctic deep sea psychrotolerant Pseudomonas stutzeri strain 7193

Lookup NU author(s): Jinwei Zhang


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Psychrotolerant Pseudomonas stutzeri strain 7193 capable of producing an extracellular α-amylase was isolated from deep sea sediments of Prydz Bay, Antarctic. The 59678-Da protein (AmyP) was encoded by 1665-bp gene (amyP). The deduced amino acid sequence was identified with four regions, which are conserved in amylolytic enzymes and form a catalytic domain, and was predicted to be maltotetraose forming extracellular amylase by using the I-TASSER online server. Purification of AmyP amylases from both the recombinant of Escherichia coli Top 10 F′ and strain 7193 was conducted. Biochemical characterization revealed that the optimal amylase activity was observed at pH 9.0 and temperature 40°C. The enzymes were unstable at temperatures above 30°C, and only retain half of their highest activity after incubation at 60°C for 5 min. Thin-layer chromatography analysis of the products of the amylolytic reaction showed the presence of maltotetraose, maltotriose, maltose and glucose in the starch hydrolysate. © 2010 Springer Science+Business Media B.V.

Publication metadata

Author(s): Zhang J, Zeng R

Publication type: Article

Publication status: Published

Journal: World Journal of Microbiology and Biotechnology

Year: 2010

Volume: 27

Issue: 4

Pages: 1573-0972

Print publication date: 19/08/2010

ISSN (print): 0959-3993

ISSN (electronic): 1573-0972

Publisher: Springer


DOI: 10.1007/s11274-010-0526-0


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